CN108387745B - Application of CD4+ T lymphocyte characteristic protein in identification of latent tuberculosis infection and active tuberculosis - Google Patents
Application of CD4+ T lymphocyte characteristic protein in identification of latent tuberculosis infection and active tuberculosis Download PDFInfo
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Abstract
The invention discloses application of CD4+ T lymphocyte characteristic protein in identifying active tuberculosis and latent tuberculosis infection. The invention provides application of a substance for detecting the expression quantity of integrin beta-3 and/or integrin-linked kinase in preparing products for distinguishing or identifying or assisting in distinguishing or identifying active tuberculosis patients and tuberculosis latent infectors. The invention discovers that integrin beta-3 and integrin-linked kinase proteins can distinguish LTBI patients from primarily treated active tuberculosis patients, and provides a new diagnosis standard for diagnosing the LTBI patients and primarily treated active tuberculosis patients.
Description
Technical Field
The invention belongs to the technical field of biology, and particularly relates to application of CD4+ T lymphocyte characteristic protein in identification of active tuberculosis and latent tuberculosis infection.
Background
The world health organization in 2015 defined LTBI as a state in which there was no clinical manifestation of active tuberculosis, but the organism persisted in an immune response to MTB antigen stimulation in the "guideline for diagnosis and treatment of latent MTB (MTB) infection (1. ent TB infection). According to the world health organization, about 1/3 people worldwide infect mycobacterium tuberculosis, of which more than 95% represent latent tuberculosis infection, and of which 5-10% of LTBI infected persons eventually develop active tuberculosis, becoming the main source of infection. Many LTBI infectors are the key and difficult point of effective prevention and control of tuberculosis at present, so accurate diagnosis of latent infection of tubercle bacillus has very important significance for preventing tuberculosis.
Since the latent infected patients lack specific symptoms and there is no unified standard and method for diagnosing latent tuberculosis infection at present, it is difficult to rapidly detect the latent tuberculosis infection patients in healthy people. The methods used in clinical practice for LTBI screening are mainly: tuberculin Skin Test (TST), Interferon-gamma release assay (IGRA). TST is simple to perform, but cannot distinguish between MTB infection and bacillus Calmette-Guerin (BCG) vaccination, and is less sensitive in immunodeficient people. In areas with high prevalence of tuberculosis in China, TST can cause false positives due to widespread inoculation with BCG; and false negative easily appears in HIV infected patients, autoimmune diseases, the elderly, children and other people with low immunity. In addition, TST detection has the defects of time consumption (48-72 hours), requirement of return visit of a subject, subjective dependence of skin test operation and result explanation and the like. IGRA detects LTBI with greater specificity than TST and is not affected by BCG vaccination and non-tuberculous mycobacteria (NTM) infection. However, the current IGRA experiment only detects IFN-gamma molecule, has low sensitivity, is easily interfered by other factors of the organism, only can detect the infection of tubercle bacillus and cannot distinguish active tuberculosis infection from latent tuberculosis infection. Moreover, IGRA experiments require blood drawing to obtain lymphocytes, require professional operators and laboratories with corresponding conditions, and samples must be completed within 8 hours after collection, and thus, cannot completely replace TST at the present stage. In addition, the samples studied at the present stage are very small and there is no gold standard for diagnosing LTBI. Therefore, there is still further research on IGRA.
In addition, although there are also new markers such as: the emergence of interleukin-2 (IL-2), HSP16.3, interferon inducible protein 10(IP-10), and monocyte chemotactic protein 2(MCP-2), etc., but there is still insufficient clinical evidence.
The tubercle bacillus infection mainly causes cellular immunity, and T lymphocytes generate a series of cell factors of differentiation, proliferation, synthesis and secretion after being stimulated by antigens to generate specific cellular immunity. Among them, CD4+The T lymphocyte plays an important role in secreting lymphokines, activating and chemotactic macrophages, promoting the macrophages to completely kill mycobacterium tuberculosis and the like.
Integrins (integrins) are membrane surface adhesion molecules that mediate cell-to-cell, cell-to-extracellular matrix adhesion, and are involved in a series of important physiological and pathological processes such as cell signal transduction, growth, differentiation, apoptosis, extension and movement, inflammation, thrombosis, tumor metastasis, and wound healing. α IIb β 3 is the most studied molecule in the integrin family and is representative of the integrin family. Alpha IIb beta 3 is an integrin molecule which is most abundantly expressed on the surface of a platelet membrane and plays an important role in the hemostasis functions of platelet adhesion, aggregation, release and the like. Research shows that the signal of the integrin alpha IIb beta 3 can be divided into a signal from the inside of a membrane to the outside of the membrane and a signal from the outside of the membrane to the inside of the membrane, wherein the signal is induced by an agonist to cause platelet activation, change the conformation of the integrin alpha IIb beta 3 and enable the integrin alpha IIb beta 3 to be adhered to a ligand thereof; the latter is triggered by ligand binding to the integrin α IIb β 3 receptor to produce a series of platelet functions.
Integrin-linked kinase (ILK), an important regulatory protein in integrin signaling pathway, plays a crucial role in integrin signaling pathway activation. It is a serine/threonine protein kinase consisting of 452 amino acids and highly expressed in various tissues throughout the body, and protein domain analysis suggests that ILK contains an N-terminal Ankyrin Repeat (ARD) structure and a kinase-like structure with a C-terminal end bound to the cytoplasmic tail of integrin. It mediates signal transduction between cells and extracellular matrix (ECM) and even from cell to cell by binding with integrin subunits, thereby affecting the downstream transmission of extracellular signals and regulating cell growth, proliferation, differentiation, survival, migration, apoptosis, adhesion and invasion.
Disclosure of Invention
An object of the present invention is to provide the use of a substance for detecting the expression level of integrin beta-3 and/or integrin-linked kinase.
The substance for detecting the expression level of integrin beta-3 and/or integrin-linked kinase provided by the invention is applied to the preparation of products for distinguishing or identifying or assisting in distinguishing or identifying active tuberculosis patients and tuberculosis latent infectors.
Another object of the present invention is to provide the use of a substance for detecting the expression level of integrin alpha-IIb (integrin alpha-IIb), integrin beta-3 (integrin beta-3) and/or integrin-linked kinase.
The application of the substance for detecting the expression quantity of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase in preparing products for detecting or assisting in detecting whether the products are tuberculosis patients or not is provided;
or the substance for detecting the expression quantity of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase provided by the invention is applied to the preparation of products for detecting or assisting to detect whether the person is a tuberculosis latent infected person.
In the application, the substance for detecting the expression level of integrin alpha-IIb is 1) or 2) as follows:
1) reagents and/or instruments required for detecting the expression quantity of the integrin alpha-IIb by utilizing protein mass spectrometry;
2) reagents and/or instruments required for detecting the expression quantity of integrin alpha-IIb by using Western Blot;
and/or the substance for detecting the expression level of integrin beta-3 is the following 3) or 4):
3) reagents and/or instruments required for detecting the expression quantity of integrin beta-3 by utilizing protein mass spectrometry;
4) reagents and/or instruments required for detecting the integrin beta-3 expression quantity by using Western Blot;
and/or the substance for detecting the expression level of the integrin-linked kinase is the following 5) or 6):
5) a reagent and/or an instrument required for detecting the expression quantity of the integrins-linked kinase by utilizing protein mass spectrometry;
6) reagents and/or instruments required for detecting the expression level of integrin-linked kinase by using Western Blot.
In the application, the expression quantity of integrin alpha-IIb is CD4+Expression level in T lymphocytes;
and/or the expression level of integrin beta-3 is CD4+Expression level in T lymphocytes;
and/or the expression level of integrin-linked kinase is CD4+Expression level in T lymphocytes.
The 3 rd object of the present invention is to provide the use of a substance that distinguishes or assists in distinguishing between active tuberculosis patients and those with latent tuberculosis infection, with integrin beta-3 and/or integrin-linked kinase as a marker.
The invention provides an application of a substance which takes integrin beta-3 and/or integrin-linked kinase as a marker for distinguishing or assisting in distinguishing active tuberculosis patients and tuberculosis latent infectors in preparing products for distinguishing or assisting in distinguishing the active tuberculosis patients and the tuberculosis latent infectors;
or the invention provides the application of the substance which takes integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase as markers for detecting or assisting to detect whether the substance is a product for detecting or assisting to detect whether the substance is a patient with tuberculosis;
or the invention provides the application of the substance for detecting or assisting to detect whether the person is a latent tuberculosis infected person or not by taking integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase as markers in preparing products for detecting or assisting to detect whether the person is a latent tuberculosis infected person or not.
In the application, the substance for distinguishing or assisting to distinguish the active tuberculosis patients and the tuberculosis latent infected patients is a substance for detecting the expression quantity of integrin beta-3 and/or integrin-linked kinase;
or, the substance for detecting or assisting the detection of the pulmonary tuberculosis patient is a substance for detecting the expression level of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase;
or the substance for detecting or assisting the detection of the tuberculosis latent infected person is a substance for detecting the expression level of integrinalpha-IIb, integrinbeta-3 and/or integrinlinked kinase.
The 4 th object of the present invention is to provide the use of integrin beta-3 and/or integrin-linked kinase as a marker for distinguishing active tuberculosis patients from those with latent tuberculosis infection.
The invention provides application of integrin beta-3 and/or integrin-linked kinase as a marker for distinguishing active tuberculosis patients and tuberculosis latent infectors in distinguishing or assisting in distinguishing the active tuberculosis patients and the tuberculosis latent infectors;
or, the invention provides the application of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase as a marker for detecting or assisting to detect whether the patient is the tuberculosis patient or not in detecting or assisting to detect whether the patient is the tuberculosis patient or not;
or, the invention provides the application of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase as a marker for detecting or assisting to detect whether a patient is a tuberculosis patient or not in detecting or assisting to detect whether the patient is a tuberculosis latent infected patient or not.
The 5 th object of the present invention is to provide a substance that distinguishes or assists in distinguishing between active tuberculosis patients and those with latent tuberculosis infection.
The substance for distinguishing or assisting to distinguish the active tuberculosis patients and the tuberculosis latent infectors is a substance for detecting the expression quantity of integrin beta-3 and/or integrin-linked kinase;
or, the substance for detecting or assisting in detecting whether the substance is a substance for a patient with tuberculosis is a substance for detecting the expression level of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase;
or, the substance for detecting or assisting to detect whether the tuberculosis is a latent infected person is a substance for detecting the expression level of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase.
It is a 6 th object of the present invention to provide a method of distinguishing or aiding in distinguishing between active tuberculosis patients and those with latent tuberculosis infection.
The method provided by the invention comprises the steps of detecting the expression quantity of integrin beta-3 and/or integrin-linked kinase in a sample to be detected, and determining whether the sample to be detected is an active tuberculosis patient or a tuberculosis latent infected patient according to the expression quantity of the integrin beta-3 and/or integrin-linked kinase;
or, the method for detecting or detecting whether the patient is the patient with the pulmonary tuberculosis in an auxiliary way comprises the steps of detecting the expression level of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase in a sample to be detected, and determining whether the sample to be detected is the patient with the pulmonary tuberculosis according to the expression level of the integrin alpha-IIb, the integrin beta-3 and/or the integrin-linked kinase;
or, the method for detecting or detecting the tuberculosis latent infector in an auxiliary way comprises the steps of detecting the expression level of integrin alpha-IIb, integrin beta-3 and/or integrin-linked kinase in a sample to be detected, and determining whether the sample to be detected is the tuberculosis latent infector not according to the expression level of the integrin alpha-IIb, the integrin beta-3 and/or the integrin-linked kinase.
In the method, the sample to be detected is a mycobacterium tuberculosis infected person;
and/or the expression level of integrin alpha-IIb is CD4+Expression level in T lymphocytes;
and/or the expression level of integrin beta-3 is CD4+Expression level in T lymphocytes;
and/or the expression level of integrin-linked kinase is CD4+Expression level in T lymphocytes.
Experiments prove that the integrin alpha-IIb, the integrin beta-3 and the integrin-linked kinase protein can be used for distinguishing healthy people from LTBI patients or distinguishing healthy people from primarily treated active tuberculosis patients, more importantly, the integrin beta-3 and the integrin-linked kinase protein can be used for distinguishing LTBI patients from primarily treated active tuberculosis patients, and therefore a new diagnosis standard is provided for diagnosing the LTBI patients and primarily treated active tuberculosis patients.
Drawings
FIG. 1 is a standard curve for BCA protein quantification.
FIG. 2 shows the result of Western-based verification of CD4+ T lymphocyte signature protein.
Detailed Description
The experimental procedures used in the following examples are all conventional procedures unless otherwise specified.
Materials, reagents and the like used in the following examples are commercially available unless otherwise specified.
Example 1 differentiation of active tuberculosis from latent tuberculosis infection CD4+Discovery and application of T lymphocyte characteristic protein
The following experimental instruments were liquid chromatography-electrospray ionization tandem mass spectrometry (Q-active Thermo Finnigan), electrophoresis (Bio-rad, USA), MultiSkans plate reader (Thermo, USA).
First, CD4+Collection of T lymphocytes
Blood samples of 9 cases each were collected from patients who had been clinically diagnosed with LTBI, patients who had been clinically diagnosed for the first treatment of active tuberculosis (to prevent the drug from affecting the body), and healthy controls. All blood samples were drawn in the early morning on an empty stomach and 5.0ml of peripheral blood was collected using a disposable vacuum anticoagulation tube.
Peripheral Blood Mononuclear Cell (PBMC) cells were extracted with lymphocyte isolate (Lymphoprep, Stemcell) within 2 hours, followed by isolation of CD4+T lymphocyte (CD 4)+T Cell Isolation Kit, Miltenyi), flow cytometry extracted CD4 was detected+The purity of T lymphocyte is 94.71%.
Second, mass spectrometric detection of CD4+T lymphocyte signature proteins
1. Protein extraction
1) Pre-cooling mortar in-20 deg.C refrigerator, taking out frozen CD4 from-80 deg.C refrigerator+T lymphocyte cell samples.
2) The cell suspension is transferred into a precooled centrifugal tube without a heat source, and is added into 0.3ml of protein lysate for full oscillation, so that the cells are dispersed and broken to the maximum extent until the solution is transparent and uniform.
3) Add 0.1ml of protein lysate and shake together until no visible suspension is visible, transfer to a pre-chilled 1.5ml tube.
4) And (5) detecting whether the volume of each tube of the ground objects is consistent or not, and not finding that the ground objects are too few.
5) The ultrasonication was set to 2 seconds at intervals of 10 seconds for 5 times and the whole operation was carried out on ice.
6) The sonicated material was placed on ice for 20 minutes, centrifuged at 10,000g for 30 minutes at 4 ℃ and the supernatant was transferred to a new tube to obtain CD4 from 9 patients with LTBI+T lymphocyte protein, CD4 from 9 patients with primary treatment of active tuberculosis+T lymphocyte protein and CD4 derived from 9 healthy controls+T lymphocyte protein, stored in a refrigerator at-80 ℃.
The formula of the protein lysate comprises: 8.0M Urea 100mM Tris-HCl pH 8.010 mM DTT 1 Xprotease inhibitor (Roche).
2. Protein quantification
CD4 from 9 LTBI patients extracted from above 1+T lymphocyte protein, CD4 from 9 patients with primary treatment of active tuberculosis+T lymphocyte protein and CD4 derived from 9 healthy controls+The T lymphocyte protein is respectively taken as the protein to be detected to be quantitatively detected as follows:
1) the final total protein amounts were 0. mu.g, 2.5. mu.g, 5. mu.g, 10. mu.g, 15. mu.g, 20. mu.g and 25. mu.g, respectively, and two detection points were set for the same protein concentration calibration curve.
2) Protein solution was prepared according to the calculation and BCA was added in a calculated volume, with a total volume of 25. mu.l. At the same time, 1ul of sample is prepared and mixed with 25ul of water.
3) According to the following weight ratio of 50: 1, uniformly mixing the solution A and the solution B of the BCA reagent to generate a working solution, adding 200 mu l of the working solution into each tube, and uniformly mixing. Adding a detection enzyme label plate.
4) Incubate at 37 ℃ for 30 minutes, then allow to stand at room temperature for 5 minutes. The presence of a purple gradient was visually observed. If the gradient is not obvious, the next detection is terminated.
5) The detection was carried out by a microplate reader (BioTek Co., Ltd.) and the detection wavelength was set at 562 nm.
6) And generating a standard curve according to the detection result, if the correlation R is less than 0.90, the standard curve cannot be used for calculation, and carrying out the experiment again.
7) According to a standard curve (fig. 1, linear formula: Y0.05422X +0.14396, R2 0.9984) to derive the total amount of test protein and calculate the corresponding concentration.
Note that:
1. the preparation before the detection of the protein sample ensures that the sample is fully dissolved, has no suspended matters and turbidity, has no precipitate after standing, and uses a buffer substance compatible with the BCA reagent.
2. The total amount of the protein to be detected is adjusted within the detection interval according to the amount of the starting material of the sample.
The results are shown in Table 1, where sample numbers 1-3 are the pool of 9 normal 3 specimens, sample numbers 4-6 are the pool of 9 latent tuberculosis infected 3 specimens, and sample numbers 7-9 are the pool of 9 active tuberculosis 3 specimens.
Table 1 shows the sample concentration and total amount distribution measured by BCA protein quantitation method
3. Trypsin enzymolysis sample
(1) Putting 200 mu g of protein solution into a centrifuge tube, and fixing the system to 125 mu l by 8M urea solution after 2 quantification;
(2) adding 5 mul of 1M DTT solution prepared in situ into the system, mixing uniformly, and incubating for 1h at 37 ℃;
(3) adding 20 mul of 1M IAA solution prepared in situ into the system, uniformly mixing, keeping out of the sun, and reacting for 1h at room temperature (25 ℃);
(4) sucking all samples, adding the samples into a 10kD ultrafiltration tube, centrifuging at 12000rpm (no more than 14000g) for 20min, and discarding the solution at the bottom of the collection tube;
(5) add 100. mu.l urea solution (8M) to the ultrafiltration tube, centrifuge at 12000rpm for 10min, and repeat 2 times.
(6) Adding 2-4 μ g (with the mass ratio of 1:50-100) of trypsin (100U/μ g) into an ultrafiltration tube, reacting at 37 ℃ for 20h at 50 μ l; and centrifuging at 12000rpm for 20min the next day, centrifuging the peptide fragment solution after enzymolysis and digestion, and collecting the precipitate at the bottom of the tube to obtain an enzymolysis product.
4. Liquid phase fractionation and protein mass spectrometry detection
The enzymatic hydrolysate obtained in 3 above was collected and 10. mu.g of the product was subjected to LCMSMS analysis according to the quantitative results. Separation was carried out using a nano liter flow rate HPLC liquid phase system EASY-nLC 1000. The liquid phase A was an aqueous solution containing 2% (by volume) acetonitrile and 0.1% (by volume) formic acid (i.e., the composition was 2ml acetonitrile, 0.1ml formic acid, and the balance water, calculated on the basis of 100 ml), and the liquid phase B was an aqueous solution containing 84% (by volume) acetonitrile and 0.1% (by volume) formic acid (i.e., the composition was 84ml acetonitrile, 0.1ml formic acid, and the balance water, calculated on the basis of 100 ml). The column Thermo EASY column SC200150 μm × 100mm (RP-C18) was equilibrated with 100% of solution A. Samples were loaded onto Thermo EASY column SC001 taps 150 μm.times.20 mm (RP-C18) (Thermo) by an autosampler and separated by chromatography at a flow rate of 400 nl/min. The relevant liquid phase gradients are as follows: 0min-100min, the linear gradient of the B liquid is from 0% to 45% (volume percentage content, the same below); 100min-108min, the linear gradient of the liquid B is from 45% to 100%; 108min-120min, and maintaining the solution B at 100%. The enzymolysis product is separated by capillary high performance liquid chromatography and then is subjected to mass spectrometry by using a Q-exact mass spectrometer (Thermo Finnigan). Analysis duration: 120min, detection mode: positive ion, parent ion scan range: 300-1800m/z, mass-to-charge ratios of polypeptides and fragments of polypeptides were collected as follows: 10 fragment patterns (MS2scan, HCD) were acquired after each full scan (full scan). The resolution of MS 1at M/Z200 is 70000, and the resolution of MS2 at M/Z200 is 17500.
5. Identification by mass spectrometry
First, the primary mass spectrum quantitative information is extracted by using Trans-genomic Pipeline software (adopting software default parameters), and the quantification is carried out by using Profile analysis2.0 software (adopting software default parameters). Then, the ProteinScaphe 2.1 software is used for data retrieval and integration, and the details are as follows:
and screening and filtering the data by using Peptide FDR (full-automatic detection) of less than or equal to 0.05. Maxquant software (part of ProteinScaphe 2.1 software) was introduced for Label-free analysis. The main parameters are as follows:
Main search ppm:6Missed cleavage:2
MS/MS tolerance ppm:20De-Isotopic:TRUE
enzyme:Trypsin database:ipi.human.3.87.fasta
Fixed modification:Carbamidomethyl(C)
Variable modification:Oxidation(M),Acetyl(Protein N-term)
Decoy database pattern:reverse
Lable free quantification(LFQ):TRUE
LFQ min ratio count:2
Match between runs:2min
Peptide FDR:0.05
Protein FDR:0.05
3 different proteins with fold change (ratio) > 1.5 or <0.6 are screened, so as to obtain a characteristic spectrum for distinguishing the proteins of the patients. Wherein, the protein with the ratio more than 1.5 is the protein with up-regulated expression, the protein with the ratio less than 0.6 is the protein with down-regulated expression, and the ratio is the ratio of the average expression quantity of the corresponding protein of the A patient to the average expression quantity of the corresponding protein of the B patient.
The finally obtained protein characteristic spectrum for distinguishing the patients A and B contains 4 proteins with expression difference, and the proteins with difference in comparison between the patients A and B comprise proteins with up-regulated expression and proteins with down-regulated expression.
The results are shown in Table 2 below,
table 2 shows proteins that differ among 3 groups of patients
It can be seen that the proteins with differential expression in the LTBI group and the active tuberculosis group are upregulated proteins compared to the healthy control group: integrin alpha-IIb (integrin alpha-IIb, sequence 1), integrin beta-3 (integrin beta-3, sequence 2), integrin-linked kinase (integrin linked kinase, sequence 3); wherein, the integrin beta-3 and the integrin-linked kinase can also effectively distinguish LTBI patients from active tuberculosis patients, and the expression level is higher in the active tuberculosis patients (P < 0.0001).
The threshold value calculation formula is as follows: relative expression of LTBI group/relative expression of healthy group
Distinguishing threshold values of health and LTBI, wherein if the relative expression level of integrin alpha-IIb in the sample to be detected is more than 2.59, the relative expression level of integrin beta-3 is more than 3.70 and/or the relative expression level of integrin kinase is more than 1.58 (at least one of the expression levels is met), the sample to be detected is LTBI, and if the condition is not met, the sample to be detected is healthy;
the threshold value calculation formula is as follows: relative expression of pulmonary tuberculosis group/relative expression of healthy group
Distinguishing threshold values (including activity and LTBI) of healthy and tuberculosis patients, if the relative expression level of integrin alpha-IIb in the sample to be detected is more than 3.04, the relative expression level of integrin beta-3 is more than 5.50 and/or the relative expression level of integrin kinase is more than 2.42 (at least one of the expression levels is met), determining that the sample to be detected is the tuberculosis patient, and if the condition is not met, determining that the sample to be detected is healthy;
the threshold value calculation formula is as follows: relative expression of pulmonary tuberculosis group/relative expression of LTBI group
And (3) distinguishing the LTBI from the active tuberculosis patient, if the relative expression level of integrin beta-3 in the sample to be detected is more than 1.49 and/or the relative expression level of integrin-linked kinase is more than 1.54 (at least one of the expression levels is met), determining that the sample to be detected is the LTBI patient, and if the condition is not met, determining that the sample to be detected is the active tuberculosis patient.
Third, Western verification of CD4+ T lymphocyte characteristic protein
1. Reagent and consumable
2. Extraction of cell proteins
Precooling RIPA protein extraction reagent, and adding protease inhibitor (phosphatase inhibitor is required to be added simultaneously for phosphorylation protein). 0.1M PMSF stock solution was added before the start of protein extraction, PMSF final concentration 1 mM. Cell count, in number of cells 1X 107To the above-mentioned one collected each group of CDs 4+The T lymphocytes are added with 1ml of lysate, the cells are fully suspended by blowing with a gun head, and after completion, the cells are incubated on ice for 20min, centrifuged at 4 ℃, and centrifuged at 13000rpm for 20 min. And (4) after centrifugation, taking the supernatant, subpackaging and storing to obtain the protein.
BCA method proteinQuantification, results from CD4 of 9 patients with LTBI+T lymphocyte protein, CD4 from 9 patients with primary treatment of active tuberculosis+T lymphocyte protein and CD4 derived from 9 healthy controls+The amounts of T lymphocyte proteins are shown in Table 1, respectively.
3. WB detection of target protein
According to the molecular weight of the target protein, 12% and 8% of separation gel is prepared, and the concentration of the concentrated gel is 5%. Loading amount of the protein sample to be detected: 10 ug/well. Electrophoresis conditions: the concentrated gel has constant pressure of 90V for about 20 min; the separation gel was kept at a constant pressure of 160V and the electrophoresis stop time was determined by prestained protein marker. Wet transfer method, transfer conditions: 300mA constant current, a NC membrane with the aperture of 0.45um and the membrane rotating time of 2 h. And dyeing the membrane by using a ponceau red dyeing reagent after the membrane transferring is finished, and observing the membrane transferring effect. And (3) sealing: the membrane was completely immersed in 3% BSA-TBST and shaken gently at room temperature for 30 min. Primary antibody incubation: the primary antibody was diluted with 3% BSA-TBST, incubated for 10min at room temperature, and left overnight at 4 ℃.
Table 4 names of the primary antibodies used
Numbering | First antibody name | Dilution ratio | Volume after |
1 | Mrp8 | 1:2000 | 4ml |
2 | COX5B | 1:1000 | 4ml |
3 | BCS1L | 1:1000 | 4ml |
4 | CD7 | 1:2000 | 4ml |
The next day the membranes were removed from 4 degrees and incubated at room temperature for 30 min. Washing the membrane: the membrane was washed 5 times with TBST, 3min each time. And (3) secondary antibody incubation: the secondary antibody was diluted with 5% skimmed milk powder-TBST, goat anti-rabbit IgG (H + L) HRP, and gently shaken at room temperature 1:10000 for 40 min. Washing the membrane: the membrane was washed 6 times with TBST, 3min each time. ECL is added on the membrane and reacts for 3-5min, and the film is exposed: 10s-5min (exposure time is adjusted according to different light intensities), developing for 2min, and fixing.
The results after film scanning were as follows:
official experiment of reference protein WB
Washing the membrane with striping Buffer at 37 deg.C for 30min (if the molecular weight difference between the target protein and the reference protein is above 10K, the step of washing the membrane with striping Buffer can be omitted).
Washing the membrane: the membrane was washed 3 times with deionized water.
Washing the membrane: washing membrane with TBST for 3 times, each for 3min
The membrane was completely immersed in 5% skimmed milk powder-TBST and gently shaken at room temperature for 30 min.
Incubation internal reference: GAPDH murine mab was added, the antibody diluted with 5% skim milk powder-TBST, 1: 20000 dilution and incubation at room temperature for 40 min.
Washing the membrane: the membrane was washed 5 times with TBST, 3min each time.
And (3) secondary antibody incubation: the secondary antibody was diluted with 5% skim milk powder-TBST, goat anti-mouse IgG (H + L) HRP, 1:10000, and gently shaken at room temperature for 40 min.
Washing the membrane: the membrane was washed 5 times with TBST, 3min each time.
ECL is added on the membrane and reacts for 3-5min, and the film is exposed: 10s-5min (exposure time is adjusted according to different light intensities), developing for 2min, and fixing.
Relative expression quantity is the gray value of target protein/GAPDH gray value
The results are shown in FIG. 2, and it can be seen that the relative expression levels of integrin alpha-IIb, integrin beta-3 and integrin-linked kinase can distinguish LTBI groups from healthy control groups; the relative expression levels of integrin beta-3 and integrin-linked kinase allow differentiation between LTBI patients and active tuberculosis patients.
Sequence listing
<110> Beijing thoracic Hospital affiliated to capital medical university
Application of <120> CD4+ T lymphocyte characteristic protein in identification of latent tuberculosis infection and active tuberculosis
<160> 3
<170> PatentIn version 3.5
<210> 1
<211> 1039
<212> PRT
<213> Artificial sequence
<400> 1
Met Ala Arg Ala Leu Cys Pro Leu Gln Ala Leu Trp Leu Leu Glu Trp
1 5 10 15
Val Leu Leu Leu Leu Gly Pro Cys Ala Ala Pro Pro Ala Trp Ala Leu
20 25 30
Asn Leu Asp Pro Val Gln Leu Thr Phe Tyr Ala Gly Pro Asn Gly Ser
35 40 45
Gln Phe Gly Phe Ser Leu Asp Phe His Lys Asp Ser His Gly Arg Val
50 55 60
Ala Ile Val Val Gly Ala Pro Arg Thr Leu Gly Pro Ser Gln Glu Glu
65 70 75 80
Thr Gly Gly Val Phe Leu Cys Pro Trp Arg Ala Glu Gly Gly Gln Cys
85 90 95
Pro Ser Leu Leu Phe Asp Leu Arg Asp Glu Thr Arg Asn Val Gly Ser
100 105 110
Gln Thr Leu Gln Thr Phe Lys Ala Arg Gln Gly Leu Gly Ala Ser Val
115 120 125
Val Ser Trp Ser Asp Val Ile Val Ala Cys Ala Pro Trp Gln His Trp
130 135 140
Asn Val Leu Glu Lys Thr Glu Glu Ala Glu Lys Thr Pro Val Gly Ser
145 150 155 160
Cys Phe Leu Ala Gln Pro Glu Ser Gly Arg Arg Ala Glu Tyr Ser Pro
165 170 175
Cys Arg Gly Asn Thr Leu Ser Arg Ile Tyr Val Glu Asn Asp Phe Ser
180 185 190
Trp Asp Lys Arg Tyr Cys Glu Ala Gly Phe Ser Ser Val Val Thr Gln
195 200 205
Ala Gly Glu Leu Val Leu Gly Ala Pro Gly Gly Tyr Tyr Phe Leu Gly
210 215 220
Leu Leu Ala Gln Ala Pro Val Ala Asp Ile Phe Ser Ser Tyr Arg Pro
225 230 235 240
Gly Ile Leu Leu Trp His Val Ser Ser Gln Ser Leu Ser Phe Asp Ser
245 250 255
Ser Asn Pro Glu Tyr Phe Asp Gly Tyr Trp Gly Tyr Ser Val Ala Val
260 265 270
Gly Glu Phe Asp Gly Asp Leu Asn Thr Thr Glu Tyr Val Val Gly Ala
275 280 285
Pro Thr Trp Ser Trp Thr Leu Gly Ala Val Glu Ile Leu Asp Ser Tyr
290 295 300
Tyr Gln Arg Leu His Arg Leu Arg Gly Glu Gln Met Ala Ser Tyr Phe
305 310 315 320
Gly His Ser Val Ala Val Thr Asp Val Asn Gly Asp Gly Arg His Asp
325 330 335
Leu Leu Val Gly Ala Pro Leu Tyr Met Glu Ser Arg Ala Asp Arg Lys
340 345 350
Leu Ala Glu Val Gly Arg Val Tyr Leu Phe Leu Gln Pro Arg Gly Pro
355 360 365
His Ala Leu Gly Ala Pro Ser Leu Leu Leu Thr Gly Thr Gln Leu Tyr
370 375 380
Gly Arg Phe Gly Ser Ala Ile Ala Pro Leu Gly Asp Leu Asp Arg Asp
385 390 395 400
Gly Tyr Asn Asp Ile Ala Val Ala Ala Pro Tyr Gly Gly Pro Ser Gly
405 410 415
Arg Gly Gln Val Leu Val Phe Leu Gly Gln Ser Glu Gly Leu Arg Ser
420 425 430
Arg Pro Ser Gln Val Leu Asp Ser Pro Phe Pro Thr Gly Ser Ala Phe
435 440 445
Gly Phe Ser Leu Arg Gly Ala Val Asp Ile Asp Asp Asn Gly Tyr Pro
450 455 460
Asp Leu Ile Val Gly Ala Tyr Gly Ala Asn Gln Val Ala Val Tyr Arg
465 470 475 480
Ala Gln Pro Val Val Lys Ala Ser Val Gln Leu Leu Val Gln Asp Ser
485 490 495
Leu Asn Pro Ala Val Lys Ser Cys Val Leu Pro Gln Thr Lys Thr Pro
500 505 510
Val Ser Cys Phe Asn Ile Gln Met Cys Val Gly Ala Thr Gly His Asn
515 520 525
Ile Pro Gln Lys Leu Ser Leu Asn Ala Glu Leu Gln Leu Asp Arg Gln
530 535 540
Lys Pro Arg Gln Gly Arg Arg Val Leu Leu Leu Gly Ser Gln Gln Ala
545 550 555 560
Gly Thr Thr Leu Asn Leu Asp Leu Gly Gly Lys His Ser Pro Ile Cys
565 570 575
His Thr Thr Met Ala Phe Leu Arg Asp Glu Ala Asp Phe Arg Asp Lys
580 585 590
Leu Ser Pro Ile Val Leu Ser Leu Asn Val Ser Leu Pro Pro Thr Glu
595 600 605
Ala Gly Met Ala Pro Ala Val Val Leu His Gly Asp Thr His Val Gln
610 615 620
Glu Gln Thr Arg Ile Val Leu Asp Cys Gly Glu Asp Asp Val Cys Val
625 630 635 640
Pro Gln Leu Gln Leu Thr Ala Ser Val Thr Gly Ser Pro Leu Leu Val
645 650 655
Gly Ala Asp Asn Val Leu Glu Leu Gln Met Asp Ala Ala Asn Glu Gly
660 665 670
Glu Gly Ala Tyr Glu Ala Glu Leu Ala Val His Leu Pro Gln Gly Ala
675 680 685
His Tyr Met Arg Ala Leu Ser Asn Val Glu Gly Phe Glu Arg Leu Ile
690 695 700
Cys Asn Gln Lys Lys Glu Asn Glu Thr Arg Val Val Leu Cys Glu Leu
705 710 715 720
Gly Asn Pro Met Lys Lys Asn Ala Gln Ile Gly Ile Ala Met Leu Val
725 730 735
Ser Val Gly Asn Leu Glu Glu Ala Gly Glu Ser Val Ser Phe Gln Leu
740 745 750
Gln Ile Arg Ser Lys Asn Ser Gln Asn Pro Asn Ser Lys Ile Val Leu
755 760 765
Leu Asp Val Pro Val Arg Ala Glu Ala Gln Val Glu Leu Arg Gly Asn
770 775 780
Ser Phe Pro Ala Ser Leu Val Val Ala Ala Glu Glu Gly Glu Arg Glu
785 790 795 800
Gln Asn Ser Leu Asp Ser Trp Gly Pro Lys Val Glu His Thr Tyr Glu
805 810 815
Leu His Asn Asn Gly Pro Gly Thr Val Asn Gly Leu His Leu Ser Ile
820 825 830
His Leu Pro Gly Gln Ser Gln Pro Ser Asp Leu Leu Tyr Ile Leu Asp
835 840 845
Ile Gln Pro Gln Gly Gly Leu Gln Cys Phe Pro Gln Pro Pro Val Asn
850 855 860
Pro Leu Lys Val Asp Trp Gly Leu Pro Ile Pro Ser Pro Ser Pro Ile
865 870 875 880
His Pro Ala His His Lys Arg Asp Arg Arg Gln Ile Phe Leu Pro Glu
885 890 895
Pro Glu Gln Pro Ser Arg Leu Gln Asp Pro Val Leu Val Ser Cys Asp
900 905 910
Ser Ala Pro Cys Thr Val Val Gln Cys Asp Leu Gln Glu Met Ala Arg
915 920 925
Gly Gln Arg Ala Met Val Thr Val Leu Ala Phe Leu Trp Leu Pro Ser
930 935 940
Leu Tyr Gln Arg Pro Leu Asp Gln Phe Val Leu Gln Ser His Ala Trp
945 950 955 960
Phe Asn Val Ser Ser Leu Pro Tyr Ala Val Pro Pro Leu Ser Leu Pro
965 970 975
Arg Gly Glu Ala Gln Val Trp Thr Gln Leu Leu Arg Ala Leu Glu Glu
980 985 990
Arg Ala Ile Pro Ile Trp Trp Val Leu Val Gly Val Leu Gly Gly Leu
995 1000 1005
Leu Leu Leu Thr Ile Leu Val Leu Ala Met Trp Lys Val Gly Phe
1010 1015 1020
Phe Lys Arg Asn Arg Pro Pro Leu Glu Glu Asp Asp Glu Glu Gly
1025 1030 1035
Glu
<210> 2
<211> 788
<212> PRT
<213> Artificial sequence
<400> 2
Met Arg Ala Arg Pro Arg Pro Arg Pro Leu Trp Ala Thr Val Leu Ala
1 5 10 15
Leu Gly Ala Leu Ala Gly Val Gly Val Gly Gly Pro Asn Ile Cys Thr
20 25 30
Thr Arg Gly Val Ser Ser Cys Gln Gln Cys Leu Ala Val Ser Pro Met
35 40 45
Cys Ala Trp Cys Ser Asp Glu Ala Leu Pro Leu Gly Ser Pro Arg Cys
50 55 60
Asp Leu Lys Glu Asn Leu Leu Lys Asp Asn Cys Ala Pro Glu Ser Ile
65 70 75 80
Glu Phe Pro Val Ser Glu Ala Arg Val Leu Glu Asp Arg Pro Leu Ser
85 90 95
Asp Lys Gly Ser Gly Asp Ser Ser Gln Val Thr Gln Val Ser Pro Gln
100 105 110
Arg Ile Ala Leu Arg Leu Arg Pro Asp Asp Ser Lys Asn Phe Ser Ile
115 120 125
Gln Val Arg Gln Val Glu Asp Tyr Pro Val Asp Ile Tyr Tyr Leu Met
130 135 140
Asp Leu Ser Tyr Ser Met Lys Asp Asp Leu Trp Ser Ile Gln Asn Leu
145 150 155 160
Gly Thr Lys Leu Ala Thr Gln Met Arg Lys Leu Thr Ser Asn Leu Arg
165 170 175
Ile Gly Phe Gly Ala Phe Val Asp Lys Pro Val Ser Pro Tyr Met Tyr
180 185 190
Ile Ser Pro Pro Glu Ala Leu Glu Asn Pro Cys Tyr Asp Met Lys Thr
195 200 205
Thr Cys Leu Pro Met Phe Gly Tyr Lys His Val Leu Thr Leu Thr Asp
210 215 220
Gln Val Thr Arg Phe Asn Glu Glu Val Lys Lys Gln Ser Val Ser Arg
225 230 235 240
Asn Arg Asp Ala Pro Glu Gly Gly Phe Asp Ala Ile Met Gln Ala Thr
245 250 255
Val Cys Asp Glu Lys Ile Gly Trp Arg Asn Asp Ala Ser His Leu Leu
260 265 270
Val Phe Thr Thr Asp Ala Lys Thr His Ile Ala Leu Asp Gly Arg Leu
275 280 285
Ala Gly Ile Val Gln Pro Asn Asp Gly Gln Cys His Val Gly Ser Asp
290 295 300
Asn His Tyr Ser Ala Ser Thr Thr Met Asp Tyr Pro Ser Leu Gly Leu
305 310 315 320
Met Thr Glu Lys Leu Ser Gln Lys Asn Ile Asn Leu Ile Phe Ala Val
325 330 335
Thr Glu Asn Val Val Asn Leu Tyr Gln Asn Tyr Ser Glu Leu Ile Pro
340 345 350
Gly Thr Thr Val Gly Val Leu Ser Met Asp Ser Ser Asn Val Leu Gln
355 360 365
Leu Ile Val Asp Ala Tyr Gly Lys Ile Arg Ser Lys Val Glu Leu Glu
370 375 380
Val Arg Asp Leu Pro Glu Glu Leu Ser Leu Ser Phe Asn Ala Thr Cys
385 390 395 400
Leu Asn Asn Glu Val Ile Pro Gly Leu Lys Ser Cys Met Gly Leu Lys
405 410 415
Ile Gly Asp Thr Val Ser Phe Ser Ile Glu Ala Lys Val Arg Gly Cys
420 425 430
Pro Gln Glu Lys Glu Lys Ser Phe Thr Ile Lys Pro Val Gly Phe Lys
435 440 445
Asp Ser Leu Ile Val Gln Val Thr Phe Asp Cys Asp Cys Ala Cys Gln
450 455 460
Ala Gln Ala Glu Pro Asn Ser His Arg Cys Asn Asn Gly Asn Gly Thr
465 470 475 480
Phe Glu Cys Gly Val Cys Arg Cys Gly Pro Gly Trp Leu Gly Ser Gln
485 490 495
Cys Glu Cys Ser Glu Glu Asp Tyr Arg Pro Ser Gln Gln Asp Glu Cys
500 505 510
Ser Pro Arg Glu Gly Gln Pro Val Cys Ser Gln Arg Gly Glu Cys Leu
515 520 525
Cys Gly Gln Cys Val Cys His Ser Ser Asp Phe Gly Lys Ile Thr Gly
530 535 540
Lys Tyr Cys Glu Cys Asp Asp Phe Ser Cys Val Arg Tyr Lys Gly Glu
545 550 555 560
Met Cys Ser Gly His Gly Gln Cys Ser Cys Gly Asp Cys Leu Cys Asp
565 570 575
Ser Asp Trp Thr Gly Tyr Tyr Cys Asn Cys Thr Thr Arg Thr Asp Thr
580 585 590
Cys Met Ser Ser Asn Gly Leu Leu Cys Ser Gly Arg Gly Lys Cys Glu
595 600 605
Cys Gly Ser Cys Val Cys Ile Gln Pro Gly Ser Tyr Gly Asp Thr Cys
610 615 620
Glu Lys Cys Pro Thr Cys Pro Asp Ala Cys Thr Phe Lys Lys Glu Cys
625 630 635 640
Val Glu Cys Lys Lys Phe Asp Arg Gly Ala Leu His Asp Glu Asn Thr
645 650 655
Cys Asn Arg Tyr Cys Arg Asp Glu Ile Glu Ser Val Lys Glu Leu Lys
660 665 670
Asp Thr Gly Lys Asp Ala Val Asn Cys Thr Tyr Lys Asn Glu Asp Asp
675 680 685
Cys Val Val Arg Phe Gln Tyr Tyr Glu Asp Ser Ser Gly Lys Ser Ile
690 695 700
Leu Tyr Val Val Glu Glu Pro Glu Cys Pro Lys Gly Pro Asp Ile Leu
705 710 715 720
Val Val Leu Leu Ser Val Met Gly Ala Ile Leu Leu Ile Gly Leu Ala
725 730 735
Ala Leu Leu Ile Trp Lys Leu Leu Ile Thr Ile His Asp Arg Lys Glu
740 745 750
Phe Ala Lys Phe Glu Glu Glu Arg Ala Arg Ala Lys Trp Asp Thr Ala
755 760 765
Asn Asn Pro Leu Tyr Lys Glu Ala Thr Ser Thr Phe Thr Asn Ile Thr
770 775 780
Tyr Arg Gly Thr
785
<210> 3
<211> 452
<212> PRT
<213> Artificial sequence
<400> 3
Met Asp Asp Ile Phe Thr Gln Cys Arg Glu Gly Asn Ala Val Ala Val
1 5 10 15
Arg Leu Trp Leu Asp Asn Thr Glu Asn Asp Leu Asn Gln Gly Asp Asp
20 25 30
His Gly Phe Ser Pro Leu His Trp Ala Cys Arg Glu Gly Arg Ser Ala
35 40 45
Val Val Glu Met Leu Ile Met Arg Gly Ala Arg Ile Asn Val Met Asn
50 55 60
Arg Gly Asp Asp Thr Pro Leu His Leu Ala Ala Ser His Gly His Arg
65 70 75 80
Asp Ile Val Gln Lys Leu Leu Gln Tyr Lys Ala Asp Ile Asn Ala Val
85 90 95
Asn Glu His Gly Asn Val Pro Leu His Tyr Ala Cys Phe Trp Gly Gln
100 105 110
Asp Gln Val Ala Glu Asp Leu Val Ala Asn Gly Ala Leu Val Ser Ile
115 120 125
Cys Asn Lys Tyr Gly Glu Met Pro Val Asp Lys Ala Lys Ala Pro Leu
130 135 140
Arg Glu Leu Leu Arg Glu Arg Ala Glu Lys Met Gly Gln Asn Leu Asn
145 150 155 160
Arg Ile Pro Tyr Lys Asp Thr Phe Trp Lys Gly Thr Thr Arg Thr Arg
165 170 175
Pro Arg Asn Gly Thr Leu Asn Lys His Ser Gly Ile Asp Phe Lys Gln
180 185 190
Leu Asn Phe Leu Thr Lys Leu Asn Glu Asn His Ser Gly Glu Leu Trp
195 200 205
Lys Gly Arg Trp Gln Gly Asn Asp Ile Val Val Lys Val Leu Lys Val
210 215 220
Arg Asp Trp Ser Thr Arg Lys Ser Arg Asp Phe Asn Glu Glu Cys Pro
225 230 235 240
Arg Leu Arg Ile Phe Ser His Pro Asn Val Leu Pro Val Leu Gly Ala
245 250 255
Cys Gln Ser Pro Pro Ala Pro His Pro Thr Leu Ile Thr His Trp Met
260 265 270
Pro Tyr Gly Ser Leu Tyr Asn Val Leu His Glu Gly Thr Asn Phe Val
275 280 285
Val Asp Gln Ser Gln Ala Val Lys Phe Ala Leu Asp Met Ala Arg Gly
290 295 300
Met Ala Phe Leu His Thr Leu Glu Pro Leu Ile Pro Arg His Ala Leu
305 310 315 320
Asn Ser Arg Ser Val Met Ile Asp Glu Asp Met Thr Ala Arg Ile Ser
325 330 335
Met Ala Asp Val Lys Phe Ser Phe Gln Cys Pro Gly Arg Met Tyr Ala
340 345 350
Pro Ala Trp Val Ala Pro Glu Ala Leu Gln Lys Lys Pro Glu Asp Thr
355 360 365
Asn Arg Arg Ser Ala Asp Met Trp Ser Phe Ala Val Leu Leu Trp Glu
370 375 380
Leu Val Thr Arg Glu Val Pro Phe Ala Asp Leu Ser Asn Met Glu Ile
385 390 395 400
Gly Met Lys Val Ala Leu Glu Gly Leu Arg Pro Thr Ile Pro Pro Gly
405 410 415
Ile Ser Pro His Val Cys Lys Leu Met Lys Ile Cys Met Asn Glu Asp
420 425 430
Pro Ala Lys Arg Pro Lys Phe Asp Met Ile Val Pro Ile Leu Glu Lys
435 440 445
Met Gln Asp Lys
450
Claims (5)
1. The application of the substance for detecting the expression quantity of integrin beta-3 and integrin-linked kinase in preparing products for distinguishing or identifying the products for treating the patients with active tuberculosis and the patients with latent tuberculosis infection;
the expression level of integrin beta-3 is CD4+Expression level in T lymphocytes;
the expression level of the integrin-linked kinase is CD4+Expression level in T lymphocytes.
2. The application of the substance for detecting the expression quantity of integrin beta-3 and integrin-linked kinase in the preparation of products for assisting in distinguishing or identifying the initially treated active tuberculosis patients and tuberculosis latent infectors;
the expression level of integrin beta-3 is CD4+Expression level in T lymphocytes;
the expression level of the integrin-linked kinase is CD4+Expression level in T lymphocytes.
3. The application of the substances for detecting the expression quantity of integrin alpha-IIb, integrin beta-3 and integrin-linked kinase in preparing products for detecting who is primarily treating active tuberculosis patients;
or the application of the substances for detecting the expression quantity of integrin alpha-IIb, integrin beta-3 and integrin-linked kinase in the preparation of products for detecting the latent tuberculosis infectors;
the expression level of integrin alpha-IIb is CD4+Expression level in T lymphocytes;
the expression level of integrin beta-3 is CD4+Expression level in T lymphocytes;
the expression level of the integrin-linked kinase is CD4+Expression level in T lymphocytes.
4. The application of substances for detecting the expression quantity of integrin alpha-IIb, integrin beta-3 and integrin-linked kinase in preparing products for assisting in detecting who is a patient who primarily treats active tuberculosis;
or the application of the substances for detecting the expression quantity of integrin alpha-IIb, integrin beta-3 and integrin-linked kinase in the preparation of products for assisting in detecting the latent tuberculosis infectors;
the expression level of integrin alpha-IIb is CD4+Expression level in T lymphocytes;
the expression level of integrin beta-3 is CD4+Expression level in T lymphocytes;
the expression level of the integrin-linked kinase is CD4+Expression level in T lymphocytes.
5. Use according to any one of claims 1 to 4, characterized in that: the substance for detecting the expression level of integrin alpha-IIb is 1) or 2) as follows:
1) reagents and/or instruments required for detecting the expression quantity of the integrin alpha-IIb by utilizing protein mass spectrometry;
2) reagents and/or instruments required for detecting the expression quantity of integrin alpha-IIb by using Western Blot;
and/or the substance for detecting the expression level of integrin beta-3 is the following 3) or 4):
3) reagents and/or instruments required for detecting the expression quantity of integrin beta-3 by utilizing protein mass spectrometry;
4) reagents and/or instruments required for detecting the integrin beta-3 expression quantity by using Western Blot;
and/or the substance for detecting the expression level of the integrin-linked kinase is the following 5) or 6):
5) a reagent and/or an instrument required for detecting the expression quantity of the integrins-linked kinase by utilizing protein mass spectrometry;
6) reagents and/or instruments required for detecting the expression level of integrin-linked kinase by using Western Blot.
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CN201810174024.7A CN108387745B (en) | 2018-03-02 | 2018-03-02 | Application of CD4+ T lymphocyte characteristic protein in identification of latent tuberculosis infection and active tuberculosis |
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CN108387745B true CN108387745B (en) | 2020-12-15 |
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SG182951A1 (en) * | 2008-06-25 | 2012-08-30 | Baylor Res Inst | Blood transcriptional signature of mycobacterium tuberculosis infection |
CN101708147A (en) * | 2009-09-29 | 2010-05-19 | 沈阳红旗制药有限公司 | Electronic medicament administration reminder applied to tuberculosis |
CN104865377A (en) * | 2015-05-29 | 2015-08-26 | 北京海思特临床检验所有限公司 | Staining kit of micro megakaryocytes of bone marrow smear, and using method of staining kit |
CN107653313B (en) * | 2017-09-12 | 2021-07-09 | 首都医科大学附属北京胸科医院 | Application of RETN and KLK1 as tuberculosis detection markers |
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Non-Patent Citations (1)
Title |
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A dual role for integrin-linked kinase in platelets: regulating integrin function and α-granule secretion;Katherine L. Tucker et al.;《BLOOD》;20081201;第112卷(第12期);第4523-4531页 * |
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